Reviewed, UniProtKB/Swiss-Prot Q63716 (PRDX1_RAT)

Names and origin

Protein names

Recommended name:
    Peroxiredoxin-1
    EC=1.11.1.15
Alternative name(s):
    Thioredoxin peroxidase 2
    Thioredoxin-dependent peroxide reductase 2
    Heme-binding 23 kDa protein
    HBP23

Gene names

Name:	Prdx1
Synonyms:	Tdpx2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subunit structure	Homodimer; disulfide-linked, upon oxidation. May form heterodimers with AOP2.
Subcellular location	Cytoplasm. Melanosome By similarity.
Post-translational modification	Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity By similarity.
Miscellaneous	The active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin. Inactivated upon oxidative stress by overoxidation of Cys-52 to Cys-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H may be irreversibly oxidized.
Sequence similarities	Belongs to the ahpC/TSA family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Inferred from direct assay. Source: RGD
Cellular component	cytosol Ref.1 Inferred from direct assay. Source: RGD melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial matrix Inferred from direct assay. Source: RGD nuclear euchromatin Inferred from direct assay. Source: RGD nucleolus Inferred from direct assay. Source: RGD peroxisomal matrix Inferred from direct assay. Source: RGD
Molecular function	heme binding Ref.1 Inferred from physical interaction. Source: RGD peroxiredoxin activity Inferred from direct assay. Source: RGD protein homodimerization activity Ref.4 Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 199

199

Peroxiredoxin-1

PRO_0000135078

Regions

Domain

6 – 165

160

Thioredoxin

Sites

Active site

52

1

Cysteine sulfenic acid (-SOH) intermediate

Amino acid modifications

Modified residue

90

1

Phosphothreonine By similarity

Modified residue

183

1

Phosphothreonine By similarity

Modified residue

194

1

Phosphotyrosine By similarity

Disulfide bond

52

Interchain (with C-173); in linked form

Disulfide bond

173

Interchain (with C-52); in linked form

Secondary structure

1

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199

Helix Strand Turn

Details...

Beta strand

16 – 20

5

Beta strand

26 – 30

5

Helix

31 – 34

4

Beta strand

37 – 43

7

Beta strand

50 – 52

3

Helix

57 – 61

5

Helix

63 – 68

6

Beta strand

71 – 78

8

Helix

81 – 88

8

Helix

92 – 94

3

Beta strand

104 – 106

3

Helix

111 – 115

5

Beta strand

121 – 124

4

Beta strand

128 – 133

6

Beta strand

137 – 145

9

Helix

153 – 168

16

Beta strand

170 – 172

3

Turn

188 – 191

4

Helix

192 – 195

4

Sequences

	Sequence		Length	Mass (Da)
	Q63716-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BDF2D4ABA8A776DA	FASTA	199	22,109
	10 20 30 40 50 60 MSSGNAKIGH PAPSFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF VCPTEIIAFS 70 80 90 100 110 120 DRAEEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLVSDPKR TIAQDYGVLK 130 140 150 160 170 180 ADEGISFRGL FIIDDKGILR QITINDLPVG RSVDEILRLV QAFQFTDKHG EVCPAGWKPG 190 SDTIKPDVNK SKEYFSKQK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification, characterization, and cloning of a heme-binding protein (23 kDa) in rat liver cytosol." Iwahara S., Satoh H., Song D.-X., Webb J., Burlingame A.L., Nagae Y., Mueller-Eberhard U. Biochemistry 34:13398-13406(1995) [PubMed: 7577926] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver and Pituitary.
[3]	Lubec G., Afjehi-Sadat L., Diao W., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 17-35 AND 111-190, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain, Hippocampus and Spinal cord.
[4]	"Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product." Hirotsu S., Abe Y., Okada K., Nagahara N., Hori H., Nishino T., Hakoshima T. Proc. Natl. Acad. Sci. U.S.A. 96:12333-12338(1999) [PubMed: 10535922] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN OXIDIZED FORM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

D30035 mRNA. Translation: BAA06275.1.
BC058450 mRNA. Translation: AAH58450.1.
BC088118 mRNA. Translation: AAH88118.1.

IPI

IPI00211779.

PIR

I52425.

RefSeq

NP_476455.1.

UniGene

Rn.2845

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QQ2	X-ray	2.60	A/B	1-199	[»]
2Z9S	X-ray	2.90	A/B/C/D/E/F/G/H/I/J	1-199	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

4508. Rno2CysPrx01.

PTM databases

PhosphoSite

Q63716.

Proteomic databases

PRIDE

Q63716.

Genome annotation databases

Ensembl

ENSRNOG00000017194. Rattus norvegicus. [Contig view]

GeneID

117254.

KEGG

rno:117254.

NMPDR

fig|10116.3.peg.23718.

Organism-specific databases

RGD

620039. Prdx1.

Phylogenomic databases

HOVERGEN

Q63716.

OMA

Q63716. IPLVSDT.

Enzyme and pathway databases

BRENDA

1.11.1.15. 248.

Gene expression databases

GermOnline

ENSRNOG00000017194. Rattus norvegicus.

Family and domain databases

InterPro

IPR000866. Alkyl_hydroperoxide_Rdtase.
IPR019479. Peroxiredoxin_C.
IPR017936. Thioredoxin-like.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]

PROSITE

PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

620108.

Entry information

Entry name

PRDX1_RAT

Accession

Primary (citable) accession number: Q63716

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)